Abstract
Duck- and rabbit globin messenger ribonucleoprotein complexes isolated by oligo(dT) cellulose chromatography reveal an identical protein pattern-two main proteins of molecular weights of 73,000 and 49,000 daltons and minor components-whether the complexes have been liberated from polyribosomes with the EDTA- or the puromycin-high-salt method. In the globin messenger ribonucleoprotein particles of both species predominantly the protein with a molecular weight of 73,000 daltons is attached to poly(A)-containing regions of the messenger RNAs.
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